SAXS STUDIES OF METALLOPROTEINS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. (1) MtmB-MtmC complex - We were able to collect data on the MtmB complex comprised of a hexamer of MtmB subunits (6 x 60 kDa) bound to six MtmC units (29 kDa). They were able to get reasonable data for the complex. We would like to complete this study by collecting data on the MtmB hexamer alone so that we can better identify the structural differences. We have crystal structures of the MtmB hexamer and MtmC and are trying to correlate the data with MS studies also ongoing. Another notable feature is that MtmB contains the 22nd genetically encoded amino acid pyrrolysine which is used to activate substrate transfer to MtmC. (2) Thermus thermophilus carboxypeptidase -We have a paper in revision at JBC on the crystal structure of this protein. As part of the revision, they have asked us to verify its dimerization in solution. Gel filtration on related systems give an anomalous result of 83 kDa compared to the monomer 59 kDa and dimer 118 kDa.